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Volumn 158, Issue 12, 2012, Pages 2903-2916

Functional amyloid formation by Streptococcus mutans

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ADHESIN P1; AMYLOID; CONGO RED; DIRECT YELLOW 7; EPIGALLOCATECHIN GALLATE; GAMMA GLUTAMYLTRANSFERASE; PEPTIDOGLYCAN; SORTASE; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 84870320868     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.060855-0     Document Type: Article
Times cited : (116)

References (89)
  • 1
    • 51949093305 scopus 로고    scopus 로고
    • Characteristics of biofilm formation by Streptococcus mutans in the presence of saliva
    • Ahn, S. J., Ahn, S. J., Wen, Z. T., Brady, L. J. & Burne, R. A. (2008). Characteristics of biofilm formation by Streptococcus mutans in the presence of saliva. Infect Immun 76, 4259-4268.
    • (2008) Infect Immun , vol.76 , pp. 4259-4268
    • Ahn, S.J.1    Ahn, S.J.2    Wen, Z.T.3    Brady, L.J.4    Burne, R.A.5
  • 3
    • 0023199712 scopus 로고
    • Isolation and characterization of monoclonal antibodies specific for antigen P1, a major surface protein of mutans streptococci
    • Ayakawa, G. Y., Boushell, L. W., Crowley, P. J., Erdos, G. W., McArthur, W. P. & Bleiweis, A. S. (1987). Isolation and characterization of monoclonal antibodies specific for antigen P1, a major surface protein of mutans streptococci. Infect Immun 55, 2759-2767.
    • (1987) Infect Immun , vol.55 , pp. 2759-2767
    • Ayakawa, G.Y.1    Boushell, L.W.2    Crowley, P.J.3    Erdos, G.W.4    McArthur, W.P.5    Bleiweis, A.S.6
  • 5
    • 0036399746 scopus 로고    scopus 로고
    • Binding of Streptococcus mutans to extracellular matrix molecules and fibrinogen
    • Beg, A. M., Jones, M. N., Miller-Torbert, T. & Holt, R. G. (2002). Binding of Streptococcus mutans to extracellular matrix molecules and fibrinogen. Biochem Biophys Res Commun 298, 75-79.
    • (2002) Biochem Biophys Res Commun , vol.298 , pp. 75-79
    • Beg, A.M.1    Jones, M.N.2    Miller-Torbert, T.3    Holt, R.G.4
  • 6
    • 22844451606 scopus 로고    scopus 로고
    • Amyloid formation modulates the biological activity of a bacterial protein
    • Bieler, S., Estrada, L., Lagos, R., Baeza, M., Castilla, J. & Soto, C. (2005). Amyloid formation modulates the biological activity of a bacterial protein. J Biol Chem 280, 26880-26885.
    • (2005) J Biol Chem , vol.280 , pp. 26880-26885
    • Bieler, S.1    Estrada, L.2    Lagos, R.3    Baeza, M.4    Castilla, J.5    Soto, C.6
  • 7
    • 0019794583 scopus 로고
    • Nutritionally variant streptococci from patients with endocarditis: Growth parameters in a semisynthetic medium and demonstration of a chromophore
    • Bouvet, A., van de Rijn, I. & McCarty, M. (1981). Nutritionally variant streptococci from patients with endocarditis: growth parameters in a semisynthetic medium and demonstration of a chromophore. J Bacteriol 146, 1075-1082.
    • (1981) J Bacteriol , vol.146 , pp. 1075-1082
    • Bouvet, A.1    van de Rijn, I.2    McCarty, M.3
  • 8
    • 0025753107 scopus 로고
    • Restriction fragment length polymorphisms and sequence variation within the spaP gene of Streptococcus mutans serotype c isolates
    • Brady, L. J., Crowley, P. J., Ma, J. K., Kelly, C., Lee, S. F., Lehner, T. & Bleiweis, A. S. (1991). Restriction fragment length polymorphisms and sequence variation within the spaP gene of Streptococcus mutans serotype c isolates. Infect Immun 59, 1803-1810.
    • (1991) Infect Immun , vol.59 , pp. 1803-1810
    • Brady, L.J.1    Crowley, P.J.2    Ma, J.K.3    Kelly, C.4    Lee, S.F.5    Lehner, T.6    Bleiweis, A.S.7
  • 9
    • 0031719488 scopus 로고    scopus 로고
    • Deletion of the central proline-rich repeat domain results in altered antigenicity and lack of surface expression of the Streptococcus mutans P1 adhesin molecule
    • Brady, L. J., Cvitkovitch, D. G., Geric, C. M., Addison, M. N., Joyce, J. C., Crowley, P. J. & Bleiweis, A. S. (1998). Deletion of the central proline-rich repeat domain results in altered antigenicity and lack of surface expression of the Streptococcus mutans P1 adhesin molecule. Infect Immun 66, 4274-4282.
    • (1998) Infect Immun , vol.66 , pp. 4274-4282
    • Brady, L.J.1    Cvitkovitch, D.G.2    Geric, C.M.3    Addison, M.N.4    Joyce, J.C.5    Crowley, P.J.6    Bleiweis, A.S.7
  • 11
    • 0036784103 scopus 로고    scopus 로고
    • Parkinson's: Another look
    • Broxmeyer, L. (2002). Parkinson's: another look. Med Hypotheses 59, 373-377.
    • (2002) Med Hypotheses , vol.59 , pp. 373-377
    • Broxmeyer, L.1
  • 16
    • 8844238368 scopus 로고    scopus 로고
    • Amyloidogenic domains, prions and structural inheritance: Rudiments of early life or recent acquisition?
    • Chernoff, Y. O. (2004). Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition? Curr Opin Chem Biol 8, 665-671.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 665-671
    • Chernoff, Y.O.1
  • 17
    • 0038004458 scopus 로고    scopus 로고
    • A novel class of secreted hydrophobic proteins is involved in aerial hyphaeformation in Streptomyces coelicolor by forming amyloid-like fibrils
    • Claessen, D., Rink, R., de Jong, W., Siebring, J., de Vreugd, P., Boersma, F. G., Dijkhuizen, L. & Wosten, H. A. (2003). A novel class of secreted hydrophobic proteins is involved in aerial hyphaeformation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev 17, 1714-1726.
    • (2003) Genes Dev , vol.17 , pp. 1714-1726
    • Claessen, D.1    Rink, R.2    de Jong, W.3    Siebring, J.4    de Vreugd, P.5    Boersma, F.G.6    Dijkhuizen, L.7    Wosten, H.A.8
  • 18
    • 0033008430 scopus 로고    scopus 로고
    • Virulence of a spaP mutant of Streptococcus mutans in a gnotobiotic rat model
    • Crowley, P. J., Brady, L. J., Michalek, S. M. & Bleiweis, A. S. (1999). Virulence of a spaP mutant of Streptococcus mutans in a gnotobiotic rat model. Infect Immun 67, 1201-1206.
    • (1999) Infect Immun , vol.67 , pp. 1201-1206
    • Crowley, P.J.1    Brady, L.J.2    Michalek, S.M.3    Bleiweis, A.S.4
  • 19
    • 77950941375 scopus 로고    scopus 로고
    • Amyloid-beta fibrillogenesis: Structural insight and therapeutic intervention
    • DaSilva, K. A., Shaw, J. E. & McLaurin, J. (2010). Amyloid-beta fibrillogenesis: structural insight and therapeutic intervention. Exp Neurol 223, 311-321.
    • (2010) Exp Neurol , vol.223 , pp. 311-321
    • Dasilva, K.A.1    Shaw, J.E.2    McLaurin, J.3
  • 20
    • 70350167108 scopus 로고    scopus 로고
    • Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose
    • de Jong, W., Wösten, H. A., Dijkhuizen, L. & Claessen, D. (2009). Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose. Mol Microbiol 73, 1128-1140.
    • (2009) Mol Microbiol , vol.73 , pp. 1128-1140
    • de Jong, W.1    Wösten, H.A.2    Dijkhuizen, L.3    Claessen, D.4
  • 26
    • 45249090641 scopus 로고    scopus 로고
    • Polymerizing the fibre between bacteria and host cells: The biogenesis of functional amyloid fibres
    • Epstein, E. A. & Chapman, M. R. (2008). Polymerizing the fibre between bacteria and host cells: the biogenesis of functional amyloid fibres. Cell Microbiol 10, 1413-1420.
    • (2008) Cell Microbiol , vol.10 , pp. 1413-1420
    • Epstein, E.A.1    Chapman, M.R.2
  • 27
    • 58649086297 scopus 로고    scopus 로고
    • Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly
    • Epstein, E. A., Reizian, M. A. & Chapman, M. R. (2009). Spatial clustering of the curlin secretion lipoprotein requires curli fiber assembly. J Bacteriol 191, 608-615.
    • (2009) J Bacteriol , vol.191 , pp. 608-615
    • Epstein, E.A.1    Reizian, M.A.2    Chapman, M.R.3
  • 31
    • 82955194531 scopus 로고    scopus 로고
    • Black tea theaflavins inhibit formation of toxic amyloid-b and a-synuclein fibrils
    • Grelle, G., Otto, A., Lorenz, M., Frank, R. F., Wanker, E. E. & Bieschke, J. (2011). Black tea theaflavins inhibit formation of toxic amyloid-b and a-synuclein fibrils. Biochemistry 50, 10624-10636.
    • (2011) Biochemistry , vol.50 , pp. 10624-10636
    • Grelle, G.1    Otto, A.2    Lorenz, M.3    Frank, R.F.4    Wanker, E.E.5    Bieschke, J.6
  • 32
    • 34547632008 scopus 로고    scopus 로고
    • The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization
    • Hammer, N. D., Schmidt, J. C. & Chapman, M. R. (2007). The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization. Proc Natl Acad Sci U S A 104, 12494-12499.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12494-12499
    • Hammer, N.D.1    Schmidt, J.C.2    Chapman, M.R.3
  • 33
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J. D. & Lansbury, P. T., Jr (1997). Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66, 385-407.
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 34
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
    • Heiser, V., Scherzinger, E., Boeddrich, A., Nordhoff, E., Lurz, R., Schugardt, N., Lehrach, H. & Wanker, E. E. (2000). Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy. Proc Natl Acad Sci U S A 97, 6739-6744.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6739-6744
    • Heiser, V.1    Scherzinger, E.2    Boeddrich, A.3    Nordhoff, E.4    Lurz, R.5    Schugardt, N.6    Lehrach, H.7    Wanker, E.E.8
  • 35
    • 73149094061 scopus 로고    scopus 로고
    • Targeting multiple biofilm pathways
    • Hett, E. C. & Hung, D. T. (2009). Targeting multiple biofilm pathways. Chem Biol 16, 1216-1218.
    • (2009) Chem Biol , vol.16 , pp. 1216-1218
    • Hett, E.C.1    Hung, D.T.2
  • 36
    • 39749163980 scopus 로고    scopus 로고
    • Physical basis of colors seen in Congo red-stained amyloid in polarized light
    • Howie, A. J., Brewer, D. B., Howell, D. & Jones, A. P. (2008). Physical basis of colors seen in Congo red-stained amyloid in polarized light. Lab Invest 88, 232-242.
    • (2008) Lab Invest , vol.88 , pp. 232-242
    • Howie, A.J.1    Brewer, D.B.2    Howell, D.3    Jones, A.P.4
  • 37
    • 0031015056 scopus 로고    scopus 로고
    • Structure, function and immunogenicity of streptococcal antigen I/II polypeptides
    • Jenkinson, H. F. & Demuth, D. R. (1997). Structure, function and immunogenicity of streptococcal antigen I/II polypeptides. Mol Microbiol 23, 183-190.
    • (1997) Mol Microbiol , vol.23 , pp. 183-190
    • Jenkinson, H.F.1    Demuth, D.R.2
  • 39
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay
    • Klunk, W. E., Jacob, R. F. & Mason, R. P. (1999). Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay. Anal Biochem 266, 66-76.
    • (1999) Anal Biochem , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 40
    • 0022468863 scopus 로고
    • Sucrosedependent cell adherence and cariogenicity of serotype c Streptococcus mutans
    • Koga, T., Asakawa, H., Okahashi, N. & Hamada, S. (1986). Sucrosedependent cell adherence and cariogenicity of serotype c Streptococcus mutans. J Gen Microbiol 132, 2873-2883.
    • (1986) J Gen Microbiol , vol.132 , pp. 2873-2883
    • Koga, T.1    Asakawa, H.2    Okahashi, N.3    Hamada, S.4
  • 44
    • 70349321700 scopus 로고    scopus 로고
    • D-Amino acids govern stationary phase cell wall remodeling in bacteria
    • Lam, H., Oh, D. C., Cava, F., Takacs, C. N., Clardy, J., de Pedro, M. A. & Waldor, M. K. (2009). D-Amino acids govern stationary phase cell wall remodeling in bacteria. Science 325, 1552-1555.
    • (2009) Science , vol.325 , pp. 1552-1555
    • Lam, H.1    Oh, D.C.2    Cava, F.3    Takacs, C.N.4    Clardy, J.5    de Pedro, M.A.6    Waldor, M.K.7
  • 45
    • 0035987235 scopus 로고    scopus 로고
    • Role of the Streptococcus gordonii SspB protein in the development of Porphyromonas gingivalis biofilms on streptococcal substrates
    • Lamont, R. J., El-Sabaeny, A., Park, Y., Cook, G. S., Costerton, J. W. & Demuth, D. R. (2002). Role of the Streptococcus gordonii SspB protein in the development of Porphyromonas gingivalis biofilms on streptococcal substrates. Microbiology 148, 1627-1636.
    • (2002) Microbiology , vol.148 , pp. 1627-1636
    • Lamont, R.J.1    El-Sabaeny, A.2    Park, Y.3    Cook, G.S.4    Costerton, J.W.5    Demuth, D.R.6
  • 47
    • 40549140723 scopus 로고    scopus 로고
    • Amyloidlike adhesins produced by floc-forming and filamentous bacteria in activated sludge
    • Larsen, P., Nielsen, J. L., Otzen, D. & Nielsen, P. H. (2008). Amyloidlike adhesins produced by floc-forming and filamentous bacteria in activated sludge. Appl Environ Microbiol 74, 1517-1526.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1517-1526
    • Larsen, P.1    Nielsen, J.L.2    Otzen, D.3    Nielsen, P.H.4
  • 49
    • 79958742851 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal region of Streptococcus mutans antigen I/II and characterization of salivary agglutinin adherence domains
    • Larson, M. R., Rajashankar, K. R., Crowley, P. J., Kelly, C., Mitchell, T. J., Brady, L. J. & Deivanayagam, C. (2011). Crystal structure of the C-terminal region of Streptococcus mutans antigen I/II and characterization of salivary agglutinin adherence domains. J Biol Chem 286, 21657-21666.
    • (2011) J Biol Chem , vol.286 , pp. 21657-21666
    • Larson, M.R.1    Rajashankar, K.R.2    Crowley, P.J.3    Kelly, C.4    Mitchell, T.J.5    Brady, L.J.6    Deivanayagam, C.7
  • 50
    • 0024443982 scopus 로고
    • Construction and characterization of isogenic mutants of Streptococcus mutans deficient in major surface protein antigen P1 (I/II)
    • Lee, S. F., Progulske-Fox, A., Erdos, G. W., Piacentini, D. A., Ayakawa, G. Y., Crowley, P. J. & Bleiweis, A. S. (1989). Construction and characterization of isogenic mutants of Streptococcus mutans deficient in major surface protein antigen P1 (I/II). Infect Immun 57, 3306-3313.
    • (1989) Infect Immun , vol.57 , pp. 3306-3313
    • Lee, S.F.1    Progulske-Fox, A.2    Erdos, G.W.3    Piacentini, D.A.4    Ayakawa, G.Y.5    Crowley, P.J.6    Bleiweis, A.S.7
  • 53
    • 17844367336 scopus 로고    scopus 로고
    • Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism
    • Lundmark, K., Westermark, G. T., Olsén, A. & Westermark, P. (2005). Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism. Proc Natl Acad Sci U S A 102, 6098-6102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6098-6102
    • Lundmark, K.1    Westermark, G.T.2    Olsén, A.3    Westermark, P.4
  • 54
    • 33745272257 scopus 로고    scopus 로고
    • Plaques of Alzheimer's disease originate from cysts of Borrelia burgdorferi, the Lyme disease spirochete
    • MacDonald, A. B. (2006). Plaques of Alzheimer's disease originate from cysts of Borrelia burgdorferi, the Lyme disease spirochete. Med Hypotheses 67, 592-600.
    • (2006) Med Hypotheses , vol.67 , pp. 592-600
    • Macdonald, A.B.1
  • 55
    • 0035089501 scopus 로고    scopus 로고
    • The hydrophobin EAS is largely unstructured in solution and functions by forming amyloidlike structures
    • Mackay, J. P., Matthews, J. M., Winefield, R. D., Mackay, L. G., Haverkamp, R. G. & Templeton, M. D. (2001). The hydrophobin EAS is largely unstructured in solution and functions by forming amyloidlike structures. Structure 9, 83-91.
    • (2001) Structure , vol.9 , pp. 83-91
    • Mackay, J.P.1    Matthews, J.M.2    Winefield, R.D.3    Mackay, L.G.4    Haverkamp, R.G.5    Templeton, M.D.6
  • 56
    • 0020464403 scopus 로고
    • A cloning vector able to replicate in Escherichia coli and Streptococcus sanguis
    • Macrina, F. L., Tobian, J. A., Jones, K. R., Evans, R. P. & Clewell, D. B. (1982). A cloning vector able to replicate in Escherichia coli and Streptococcus sanguis. Gene 19, 345-353.
    • (1982) Gene , vol.19 , pp. 345-353
    • Macrina, F.L.1    Tobian, J.A.2    Jones, K.R.3    Evans, R.P.4    Clewell, D.B.5
  • 57
    • 60349097590 scopus 로고    scopus 로고
    • The emerging concept of functional amyloid
    • Maury, C. P. (2009a). The emerging concept of functional amyloid. J Intern Med 265, 329-334.
    • (2009) J Intern Med , vol.265 , pp. 329-334
    • Maury, C.P.1
  • 58
    • 68049114613 scopus 로고    scopus 로고
    • Self-propagating b-sheet polypeptide structures as prebiotic informational molecular entities: The amyloid world
    • Maury, C. P. (2009b). Self-propagating b-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world. Orig Life Evol Biosph 39, 141-150.
    • (2009) Orig Life Evol Biosph , vol.39 , pp. 141-150
    • Maury, C.P.1
  • 61
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula, M., Kayed, R., Milton, S. & Glabe, C. G. (2007). Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282, 10311-10324.
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 62
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson, M. R. (2004). Techniques to study amyloid fibril formation in vitro. Methods 34, 151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 65
    • 78651091866 scopus 로고    scopus 로고
    • Structure of the Cterminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans
    • Nylander, A., Forsgren, N. & Persson, K. (2011). Structure of the Cterminal domain of the surface antigen SpaP from the caries pathogen Streptococcus mutans. Acta Crystallogr Sect F Struct Biol Cryst Commun 67, 23-26.
    • (2011) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.67 , pp. 23-26
    • Nylander, A.1    Forsgren, N.2    Persson, K.3
  • 66
    • 47049126124 scopus 로고    scopus 로고
    • Candida albicans Als adhesins have conserved amyloid-forming sequences
    • Otoo, H. N., Lee, K. G., Qiu, W. & Lipke, P. N. (2008). Candida albicans Als adhesins have conserved amyloid-forming sequences. Eukaryot Cell 7, 776-782.
    • (2008) Eukaryot Cell , vol.7 , pp. 776-782
    • Otoo, H.N.1    Lee, K.G.2    Qiu, W.3    Lipke, P.N.4
  • 67
    • 43549085062 scopus 로고    scopus 로고
    • We find them here, we find them there: Functional bacterial amyloid
    • Otzen, D. & Nielsen, P. H. (2008). We find them here, we find them there: functional bacterial amyloid. Cell Mol Life Sci 65, 910-927.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 910-927
    • Otzen, D.1    Nielsen, P.H.2
  • 68
    • 84863680519 scopus 로고    scopus 로고
    • YidC1 and YidC2 are functionally distinct proteins involved in protein secretion, biofilm formation and cariogenicity of Streptococcus mutans
    • Palmer, S. R., Crowley, P. J., Oli, M. W., Ruelf, M. A., Michalek, S. M. & Brady, L. J. (2012). YidC1 and YidC2 are functionally distinct proteins involved in protein secretion, biofilm formation and cariogenicity of Streptococcus mutans. Microbiology 158, 1702-1712.
    • (2012) Microbiology , vol.158 , pp. 1702-1712
    • Palmer, S.R.1    Crowley, P.J.2    Oli, M.W.3    Ruelf, M.A.4    Michalek, S.M.5    Brady, L.J.6
  • 69
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • Porat, Y., Abramowitz, A. & Gazit, E. (2006). Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism. Chem Biol Drug Des 67, 27-37.
    • (2006) Chem Biol Drug Des , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 71
    • 4544330112 scopus 로고    scopus 로고
    • Global cell surface conformational shift mediated by a Candida albicans adhesin
    • Rauceo, J. M., Gaur, N. K., Lee, K. G., Edwards, J. E., Klotz, S. A. & Lipke, P. N. (2004). Global cell surface conformational shift mediated by a Candida albicans adhesin. Infect Immun 72, 4948-4955.
    • (2004) Infect Immun , vol.72 , pp. 4948-4955
    • Rauceo, J.M.1    Gaur, N.K.2    Lee, K.G.3    Edwards, J.E.4    Klotz, S.A.5    Lipke, P.N.6
  • 72
    • 80051563535 scopus 로고    scopus 로고
    • A therapeutic anti-Streptococcus mutans monoclonal antibody used in human passive protection trials influences the adaptive immune response
    • Robinette, R. A., Oli, M. W., McArthur, W. P. & Brady, L. J. (2011). A therapeutic anti-Streptococcus mutans monoclonal antibody used in human passive protection trials influences the adaptive immune response. Vaccine 29, 6292-6300.
    • (2011) Vaccine , vol.29 , pp. 6292-6300
    • Robinette, R.A.1    Oli, M.W.2    McArthur, W.P.3    Brady, L.J.4
  • 73
    • 76649143766 scopus 로고    scopus 로고
    • Amyloid fibers provide structural integrity to Bacillus subtilis biofilms
    • Romero, D., Aguilar, C., Losick, R. & Kolter, R. (2010). Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. Proc Natl Acad Sci U S A 107, 2230-2234.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2230-2234
    • Romero, D.1    Aguilar, C.2    Losick, R.3    Kolter, R.4
  • 74
    • 79957460465 scopus 로고    scopus 로고
    • An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms
    • Romero, D., Vlamakis, H., Losick, R. & Kolter, R. (2011). An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms. Mol Microbiol 80, 1155-1168.
    • (2011) Mol Microbiol , vol.80 , pp. 1155-1168
    • Romero, D.1    Vlamakis, H.2    Losick, R.3    Kolter, R.4
  • 75
    • 0031932327 scopus 로고    scopus 로고
    • Curli fibers are highly conserved between Salmonella typhimurium and Escherichia coli with respect to operon structure and regulation
    • Römling, U., Bian, Z., Hammar, M., Sierralta, W. D. & Normark, S. (1998). Curli fibers are highly conserved between Salmonella typhimurium and Escherichia coli with respect to operon structure and regulation. J Bacteriol 180, 722-731.
    • (1998) J Bacteriol , vol.180 , pp. 722-731
    • Römling, U.1    Bian, Z.2    Hammar, M.3    Sierralta, W.D.4    Normark, S.5
  • 76
    • 63849126614 scopus 로고    scopus 로고
    • Synergistic role of curli and cellulose in cell adherence and biofilm formation of attaching and effacing Escherichia coli and identification of Fis as a negative regulator of curli
    • Saldaña, Z., Xicohtencatl-Cortes, J., Avelino, F., Phillips, A. D., Kaper, J. B., Puente, J. L. & Girón, J. A. (2009). Synergistic role of curli and cellulose in cell adherence and biofilm formation of attaching and effacing Escherichia coli and identification of Fis as a negative regulator of curli. Environ Microbiol 11, 992-1006.
    • (2009) Environ Microbiol , vol.11 , pp. 992-1006
    • Saldaña, Z.1    Xicohtencatl-Cortes, J.2    Avelino, F.3    Phillips, A.D.4    Kaper, J.B.5    Puente, J.L.6    Girón, J.A.7
  • 77
    • 0042737826 scopus 로고    scopus 로고
    • Identification of mutans streptococci by restriction fragment length polymorphism analysis of polymerase chain reaction-amplified 16S ribosomal RNA genes
    • Sato, T., Hu, J. P., Ohki, K., Yamaura, M., Washio, J., Matsuyama, J. & Takahashi, N. (2003). Identification of mutans streptococci by restriction fragment length polymorphism analysis of polymerase chain reaction-amplified 16S ribosomal RNA genes. Oral Microbiol Immunol 18, 323-326.
    • (2003) Oral Microbiol Immunol , vol.18 , pp. 323-326
    • Sato, T.1    Hu, J.P.2    Ohki, K.3    Yamaura, M.4    Washio, J.5    Matsuyama, J.6    Takahashi, N.7
  • 78
    • 79955452211 scopus 로고    scopus 로고
    • The assembly of individual chaplin peptides from Streptomyces coelicolor into functional amyloid fibrils
    • Sawyer, E. B., Claessen, D., Haas, M., Hurgobin, B. & Gras, S. L. (2011). The assembly of individual chaplin peptides from Streptomyces coelicolor into functional amyloid fibrils. PLoS ONE 6, e18839.
    • (2011) PLoS ONE , vol.6
    • Sawyer, E.B.1    Claessen, D.2    Haas, M.3    Hurgobin, B.4    Gras, S.L.5
  • 79
    • 0022740154 scopus 로고
    • Comparative recovery of Streptococcus mutans on five isolation media, including a new simple selective medium
    • Schaeken, M. J., van der Hoeven, J. S. & Franken, H. C. (1986). Comparative recovery of Streptococcus mutans on five isolation media, including a new simple selective medium. J Dent Res 65, 906-908.
    • (1986) J Dent Res , vol.65 , pp. 906-908
    • Schaeken, M.J.1    van der Hoeven, J.S.2    Franken, H.C.3
  • 80
    • 84864054380 scopus 로고    scopus 로고
    • Functional amyloids composed of phenol soluble modulins stabilize Staphylococcus aureus biofilms
    • Schwartz, K., Syed, A. K., Stephenson, R. E., Rickard, A. H. & Boles, B. R. (2012). Functional amyloids composed of phenol soluble modulins stabilize Staphylococcus aureus biofilms. PLoS Pathog 8, e1002744.
    • (2012) PLoS Pathog , vol.8
    • Schwartz, K.1    Syed, A.K.2    Stephenson, R.E.3    Rickard, A.H.4    Boles, B.R.5
  • 81
  • 84
    • 52849097866 scopus 로고    scopus 로고
    • Caries ecology revisited: Microbial dynamics and the caries process
    • Takahashi, N. & Nyvad, B. (2008). Caries ecology revisited: microbial dynamics and the caries process. Caries Res 42, 409-418.
    • (2008) Caries Res , vol.42 , pp. 409-418
    • Takahashi, N.1    Nyvad, B.2
  • 85
    • 8844240627 scopus 로고    scopus 로고
    • Protein sorting to the cell wall envelope of Gram-positive bacteria
    • Ton-That, H., Marraffini, L. A. & Schneewind, O. (2004). Protein sorting to the cell wall envelope of Gram-positive bacteria. Biochim Biophys Acta 1694, 269-278.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 269-278
    • Ton-That, H.1    Marraffini, L.A.2    Schneewind, O.3
  • 86
    • 0036308656 scopus 로고    scopus 로고
    • Crystal structure of the V-region of Streptococcus mutans antigen I/II at 2.4 A resolution suggests a sugar preformed binding site
    • Troffer-Charlier, N., Ogier, J., Moras, D. & Cavarelli, J. (2002). Crystal structure of the V-region of Streptococcus mutans antigen I/II at 2.4 A resolution suggests a sugar preformed binding site. J Mol Biol 318, 179-188.
    • (2002) J Mol Biol , vol.318 , pp. 179-188
    • Troffer-Charlier, N.1    Ogier, J.2    Moras, D.3    Cavarelli, J.4
  • 87
    • 44949244024 scopus 로고    scopus 로고
    • Sequence determinants of bacterial amyloid formation
    • Wang, X. & Chapman, M. R. (2008). Sequence determinants of bacterial amyloid formation. J Mol Biol 380, 570-580.
    • (2008) J Mol Biol , vol.380 , pp. 570-580
    • Wang, X.1    Chapman, M.R.2
  • 89
    • 0038309658 scopus 로고    scopus 로고
    • Production of cellulose and curli fimbriae by members of the family Enterobacteriaceae isolated from the human gastrointestinal tract
    • Zogaj, X., Bokranz, W., Nimtz, M. & Römling, U. (2003). Production of cellulose and curli fimbriae by members of the family Enterobacteriaceae isolated from the human gastrointestinal tract. Infect Immun 71, 4151-4158.
    • (2003) Infect Immun , vol.71 , pp. 4151-4158
    • Zogaj, X.1    Bokranz, W.2    Nimtz, M.3    Römling, U.4


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